| Description | This entry represents pilotin AspS from Vibrio and some E.coli and Shigella. This entry also includes YghG from E. coli. AspS is part of the Vibrio-type T2SS secretin system that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. The structure of AspS has been revealed [ , ].The type II secretion system (T2SS) is one of several extracellular secretion systems in gram-negative bacteria. It delivers toxins and a range of hydrolytic enzymes including proteases, lipases and carbohydrate-active enzymes to the cell surface or extracellular space [ ]. T2SS systems are composed of 11 to 15 different proteins, which are generally called GspA to GspO and GspS. The T2SS spans the two bacterial membranes and ensures secretion of folded proteins across the outer membrane pore formed by GspD. The inner membrane complex contains GspC, GspL, GspM, and GspF. The cytoplasmic domains of GspL and GspF interact with an ATPase, GspE. GspE is thought to energize the formation of a short pseudopilus by several pilin-like proteins, GspG to GspK []. GspD has been shown to interact with the inner membrane component GspC []. | Name | Type II secretion system (T2SS) pilotin, S protein |
| Short Name | T2SSS_2 | Type | Family |
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